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To advance our ability to model bacterial growth on such substrates, axenic cultures were grown in chemostats at a low specific growth rate and a constant total energy flux on binary and ternary substrate mixtures and were assayed for key catabolic enzymes for each substrate. The substrates were benzoate, salicylate, and glucose, and the enzymes were catechol 1,2\u2010dioxygenase, gentisate 1,2\u2010dioxygenase, and glucose\u20106\u2010phosphate dehydrogenase, respectively. The binary mixtures were salicylate with benzoate and salicylate with glucose. Measurements were also made of oxygen uptake rate by whole cells in response to each substrate. The effects of the substrate mixture on the oxygen uptake rate paralleled the effects on the measured enzymes. Catechol 1,2\u2010dioxygenase exhibited a threshold response before synthesis occurred. Below the threshold flux of benzoate through the chemostat, either basal enzyme levels or nonspecific enzymes kept reactor concentrations too low for enzyme synthesis. Above the threshold, enzyme levels were linearly related to the fraction of the total energy flux through the chemostat due to benzoate. Gentisate 1,2\u2010dioxygenase exhibited a linear response to the salicylate flux when mixed with benzoate, but a threshold response when mixed with glucose. Glucose\u20106\u2010phosphate dehydrogenase activity increased in direct proportion to the glucose flux through the chemostat over the entire range studied. The results from two ternary mixtures were consistent with those from the binary mixtures. \u00a9 2002 Wiley Periodicals, Inc. 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